Could vitamin E be bad for your bones?

Latest news from Nature journals 5 March 2012

This press release contains:

---Summaries of newsworthy papers:

Medicine: Vitamin E may be bad for bones

Neuroscience: Sensing sustained environmental threats

---Mention of papers to be published at the same time with the same embargo

---Geographical listing of authors

Warning: This document, and the Nature journal papers to which it refers, may contain information that is price sensitive (as legally defined, for example, in the UK Criminal Justice Act 1993 Part V) with respect to publicly quoted companies. Anyone dealing in securities using information contained in this document, or in advance copies of a Nature journal’s content, may be guilty of insider trading under the US Securities Exchange Act of 1934.

PICTURES: To obtain artwork from any of the journals, you must first obtain permission from the copyright holder (if named) or author of the research paper in question (if not).

NOTE: Once a paper is published, the digital object identifier (DOI) number can be used to retrieve the abstract and full text from the journal web site (abstracts are available to everyone, full text is available only to subscribers). To do this, add the DOI to the following URL: (For example, For more information about DOIs and Advance Online Publication, see

HYPE: We take great care not to hype the papers mentioned on our press releases, but are sometimes accused of doing so. If you ever consider that a story has been hyped, please do not hesitate to contact us at [email protected], citing the specific example.


[1] Medicine: Vitamin E may be bad for bones
DOI: 10.1038/nm.2659

Vitamin E decreases bone mass by stimulating the generation of bone-degrading cells, reports an article published online this week in Nature Medicine. As vitamin E containing supplements are widely consumed, these results may have public-health implications.

Bone strength is maintained by the balance between bone-forming cells, called osteoblasts, and bone-degrading cells, called osteoclasts, which are formed by the fusion of precursor cells. Although the role of fat-soluble vitamins such as vitamin D in maintaining bone strength is well known, the role of vitamin E, or alpha-tocopherol, is less clear. Early studies had shown a positive effect of vitamin E on bone. This effect was proposed to be dependent on the antioxidant properties of alpha-tocopherol.

By contrast, Shu Takeda and his colleagues report that mice deficient in an alpha-tocopherol transfer protein, a model of vitamin E deficiency, have high bone mass as a result of a decrease in bone degradation. The team found that alpha-tocopherol stimulated the fusion of osteoclast precursor cells, independently of its antioxidant capacity, by inducing the expression of a series of molecules crucial for osteoclast formation. Moreover, healthy mice or rats fed a diet with an amount of alpha-tocopherol similar to what is found in supplements consumed by many people lost bone mass, highlighting the potential relevance of these findings to human health.

Author contact:

Shu Takeda (Keio University, Tokyo, Japan)
Tel: +81 3 3353 1211; E-mail: [email protected]


[2] Neuroscience: Sensing sustained environmental threats
DOI: 10.1038/nn.3061

The mechanisms that mediate the behavior of the worm C. elegans in response to environmental oxygen concentration are described in a study published online this week in Nature Neuroscience. These results represent an important step in our understanding of how animals implement persistent defense behaviors.

All organisms have to deal with a barrage of environmental information. Sensory systems have therefore evolved adaptive mechanisms that allow them to only react briefly to most stimuli, or rapidly ignore some of them. However, certain harmful stimuli have to hold our attention for a prolonged period of time, but the mechanisms that mediate this sustained response are not fully understood.

In the wild, C. elegans is likely exposed to oxygen concentrations varying from very low to very high levels. When exposed to higher or lower oxygen concentrations, the worm responds by changing speed or direction, or by aggregating with other worms to collectively reduce oxygen concentrations. Mario De Bono and colleagues studied the oxygen-sensing neurons of the worm, called ‘tonic’ sensors, that respond continuously during oxygen exposure. Using a set of genetic tools, the scientists worked out the molecular mechanisms in these neurons that are required to generate these tonic signals, and determined how these signals are transformed in different downstream neurons to elicit short and long-term behaviors.

Author contact:

Mario De Bono (MRC Laboratory of Molecular Biology, Cambridge, UK)
Tel: +44 1223 402278; E-mail: [email protected]


Items from other Nature journals to be published online at the same time and with the same embargo:

Nature (

[3] Corticostriatal plasticity is necessary for learning intentional neuroprosthetic skills
DOI: 10.1038/nature10845

[4] Coevolution in multidimensional trait space favours escape from parasites and pathogens
DOI: 10.1038/nature10853

[5] Enzymatic catalysis of anti-Baldwin ring closure in polyether biosynthesis
DOI: 10.1038/nature10865

[6] Chromatin-modifying enzymes as modulators of reprogramming
DOI: 10.1038/nature10953


[7] CDK5 and MEKK1 mediate pro-apoptotic signalling following endoplasmic reticulum stress in an autosomal dominant retinitis pigmentosa model
DOI: 10.1038/ncb2447

[8] A size-exclusion permeability barrier and nucleoporins characterize a ciliary pore complex that regulates transport into cilia
DOI: 10.1038/ncb2450

[9] Homeostatic control of recombination is implemented progressively in mouse meiosis
DOI: 10.1038/ncb2451

[10] Lrig1 controls intestinal stem-cell homeostasis by negative regulation of ErbB signaling
DOI: 10.1038/ncb2464

[11] Fbxw7a- and GSK3-mediated degradation of p100 is a pro-survival mechanism in multiple myeloma
DOI: 10.1038/ncb2463


[12] Peptides induce persistent signaling from endosomes by a nutrient transceptor
DOI: 10.1038/nchembio.910


[13] Self-assembly of the oxy-tyrosinase core and the fundamental components of phenolic hydroxylation

[14] Metal-directed, chemically tunable assembly of one-, two- and three-dimensional crystalline protein arrays


[15] Climate response to zeroed emissions of greenhouse gases and aerosols
DOI: 10.1038/nclimate1424

[16] Reconciling top-down and bottom-up modelling on future bioenergy deployment
DOI: 10.1038/nclimate1416

[17] Trade-offs and synergies in urban climate policies
DOI: 10.1038/nclimate1434

[18] Black-carbon reduction of snow albedo
DOI: 10.1038/nclimate1433

Living in the doughnut
DOI: 10.1038/nclimate1457


[19] Mutations in axonemal dynein assembly factor DNAAF3 cause primary ciliary dyskinesia
DOI: 10.1038/ng.1106

[20] A new subtype of bone sarcoma defined by BCOR-CCNB3 gene fusion
DOI: 10.1038/ng.1107

[21] A genome-wide association study identifies two susceptibility loci for duodenal ulcer in the Japanese population
DOI: 10.1038/ng.1109

[22] Ascorbic acid prevents loss of Dlk1-Dio3 imprinting and facilitates generation of all-iPS cell mice from terminally differentiated B cells
DOI: 10.1038/ng.1110

[23] Complex reorganization and predominant non-homologous repair following chromosomal breakage in karyotypically balanced germline rearrangements and transgenic integration
DOI: 10.1038/ng.2202


[24] NF-kappaB-mediated degradation of the coactivator RIP140 regulates inflammatory responses and contributes to endotoxin tolerance

[25] NLRP4 negatively regulates type I interferon signaling by targeting the kinase TBK1 for degradation via the ubiquitin ligase DTX4


[26] On the molecular origin of supercapacitance in nanoporous carbon electrodes
DOI: 10.1038/nmat3260


[27] Tyrosine phosphatase SHP2 promotes breast cancer progression and maintains tumor-initiating cells via activation of key transcription factors and a positive feedback signaling loop
DOI: 10.1038/nm.2645

[28] Macrophage-derived Wnt opposes Notch signaling to specify hepatic progenitor cell fate in chronic liver disease
DOI: 10.1038/nm.2667

[29] IL-17A produced by alpha-beta T cells drives airway hyper-responsiveness in mice and enhances mouse and human airway smooth muscle contraction
DOI: 10.1038/nm.2684


[30] Long-term, efficient inhibition of microRNA function in mice using rAAV vectors
DOI: 10.1038/nmeth.1903

[31] TULIPs: Tunable, light-controlled interacting protein tags for cell biology
DOI: 10.1038/nmeth.1904

[32] Fast gapped read alignment with Bowtie 2
DOI: 10.1038/nmeth.1923

[33] Computerized video analysis of social interactions in mice
DOI: 10.1038/nmeth.1924


[34] The growth factor SVH-1 regulates axon regeneration in C. elegans via the JNK MAPK cascade
DOI: 10.1038/nn.3052

[35] Mitochondrial CB1 receptors regulate neuronal energy metabolism
DOI: 10.1038/nn.3053

[36] The voltage-gated proton channel, Hv1, enhances brain damage from ischemic stroke
DOI: 10.1038/nn.3059

[37] Active dendrites support efficient initiation of dendritic spikes in hippocampal CA3 pyramidal neurons
DOI: 10.1038/nn.3060


[38] Frequency comb generation at terahertz frequencies by coherent phonon excitation in silicon
DOI: 10.1038/nphoton.2012.35

[39] A comparison of graphene, superconductors and metals as conductors for metamaterials and plasmonics
DOI: 10.1038/nphoton.2012.27

[40] Heralded quantum entanglement between two crystals
DOI: 10.1038/nphoton.2012.34

Nature PHYSICS (

[41] Three-dimensional localization of ultracold atoms in an optical disordered potential
DOI: 10.1038/nphys2256

[42] Nodal superconducting-gap structure in ferropnictide superconductor BaFe2(As0.7P0.3)2
DOI: 10.1038/nphys2248

[43] Satellites and large doping and temperature dependence of electronic properties in hole-doped BaFe2As2
DOI: 10.1038/nphys2250


[44] The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex
DOI: 10.1038/nsmb.2242

[45] The SUMO protease SENP7 is a critical component to ensure HP1 enrichment at pericentric heterochromatin
DOI: 10.1038/nsmb.2244

[46] Structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site
DOI: 10.1038/nsmb.2250

[47] A sensor-adaptor mechanism for enterovirus uncoating from structures of EV71
DOI: 10.1038/nsmb.2255

[48] Topoisomerase I poisoning results in PARP-mediated replication fork reversal
DOI: 10.1038/nsmb.2258



The following list of places refers to the whereabouts of authors on the papers numbered in this release. The listing may be for an author's main affiliation, or for a place where they are working temporarily. Please see the PDF of the paper for full details.

Roseworthy: 23
Sydney: 35
Klosterneuburg: 37
Vienna: 30
Leuven: 12, 28
Burnaby: 15
Montreal: 15
Quebec: 23
Beijing: 30, 47
Chengdu: 30
Nanjing: 25
Shanghai: 42
Bordeaux: 20, 35
Orsay: 33
Palaiseau: 43
Paris: 17, 20, 26, 33, 41, 43, 44, 45
Talence: 41
Toulouse: 17
Tours: 2, 26
Berlin: 16
Heidelberg: 4
Mainz: 35
Martinsried: 44
Munster: 19
Postdam: 16
Crete: 39
Tel-Aviv: 19
Milan: 27, 48
Rome: 35
Aichi: 21
Chiba: 43
Ibaraki: 43
Kanagawa: 21
Nagoya: 34
Osaka: 1, 10
Saitama: 43
Sapporo: 5
Shizuoka: 5
Tokyo: 1, 19, 21, 38, 43
Tsukuba: 34, 38
Yokohama: 29
Amsterdam: 28
Utrecht: 10, 28
Auckland: 23
Lisbon: 3
Singapore: 5
Barcelona: 9
Leioia: 35
Madrid: 35
Salamanca: 48
Seville: 10
Jeddah: 19
Lund: 43
Basel: 27
Bern: 35
Fribourg: 43
Geneva: 40
Zurich: 43, 48
Taichung: 4
Ankara: 4
Cambridge: 2, 10
Didcot: 47
Edinburgh: 28
Faversham: 2
Glasgow: 28
Hertfordshire: 48
Leeds: 47
Leicester: 19
London: 10, 19, 22
Oxford: 5, 24, 26, 47
Berkeley: 3, 18
Chico: 13
La Jolla: 11, 14, 48
Los Angeles: 5
Menlo Park: 5
Richmond: 16
San Francisco: 29
Stanford: 13, 45
District of Columbia
Washington: 17
Moscow: 4
Chicago: 31
Evanston: 31, 46
Ames: 39
Pittsburgh: 38
Baltimore: 32
Bethesda: 3
Chevy Chase: 4
College Park: 32
Boston: 4, 22, 23, 27, 30, 36
Cambridge: 4, 22, 23
Worcester: 30
Ann Arbor: 8, 11
Minneapolis: 24
New York
New York: 7, 9, 11, 19, 22, 43
Tarrytown: 11
North Carolina
Research Triangle Park: 27
Philadelphia: 26
Knoxville: 4
Nashville: 46
Houston: 25
Salt Lake City: 34
Charlottesville: 23
Fairfax: 14



For media inquiries relating to embargo policy for all the Nature Research Journals:

Rachel Twinn (Nature London)
Tel: +44 20 7843 4658; E-mail: [email protected]

Neda Afsarmanesh (Nature New York)
Tel: +1 212 726 9231; E-mail: [email protected]

Eiji Matsuda (Nature Tokyo)
Tel: +81 3 3267 8751; E-mail: [email protected]

For media inquiries relating to editorial content/policy for the Nature Research Journals, please contact the journals individually:

Nature Biotechnology (New York)
Michael Francisco
Tel: +1 212 726 9288; E-mail: [email protected]

Nature Cell Biology (London)
Sowmya Swaminathan
Tel: +44 20 7843 4656; E-mail: [email protected]

Nature Chemical Biology (Boston)
Elissa Bolt
Tel: +1 617 475 9241, E-mail: [email protected]

Nature Chemistry (London)
Stuart Cantrill
Tel: +44 20 7014 4018; E-mail: [email protected]

Nature Climate Change (London)
Rory Howlett
Tel: +44 20 7014 4009; E-mail: [email protected]

Nature Genetics (New York)
Myles Axton
Tel: +1 212 726 9324; E-mail: [email protected]

Nature Geoscience (London)
Heike Langenberg
Tel: +44 20 7843 4042; E-mail: [email protected]

Nature Immunology (New York)
Laurie Dempsey
Tel: +1 212 726 9372; E-mail: [email protected]

Nature Materials (London)
Vincent Dusastre
Tel: +44 20 7843 4531; E-mail: [email protected]

Nature Medicine (New York)
Juan Carlos Lopez
Tel: +1 212 726 9325; E-mail: [email protected]

Nature Methods (New York)
Hugh Ash
Tel: +1 212 726 9627; E-mail: [email protected]

Nature Nanotechnology (London)
Peter Rodgers
Tel: +44 20 7014 4019; Email: [email protected]

Nature Neuroscience (New York)
Kalyani Narasimhan
Tel: +1 212 726 9319; E-mail: [email protected]

Nature Photonics (Tokyo)
Oliver Graydon
Tel: +81 3 3267 8776; E-mail: [email protected]

Nature Physics (London)
Alison Wright
Tel: +44 20 7843 4555; E-mail: [email protected]

Nature Structural & Molecular Biology (New York)
Sabbi Lall
Tel: +1 212 726 9326; E-mail: [email protected]


About Nature Publishing Group (NPG):

Nature Publishing Group (NPG) is a publisher of high impact scientific and medical information in print and online. NPG publishes journals, online databases and services across the life, physical, chemical and applied sciences and clinical medicine.

Focusing on the needs of scientists, Nature (founded in 1869) is the leading weekly, international scientific journal. In addition, for this audience, NPG publishes a range of Nature research journals and Nature Reviews journals, plus a range of prestigious academic journals including society-owned publications. Online, provides over 5 million visitors per month with access to NPG publications and online databases and services, including Nature News and NatureJobs plus access to Nature Network and Nature Education’s

Scientific American is at the heart of NPG’s newly-formed consumer media division, meeting the needs of the general public. Founded in 1845, Scientific American is the oldest continuously published magazine in the US and the leading authoritative publication for science in the general media. Together with and 15 local language editions around the world it reaches over 3 million consumers and scientists. Other titles include Scientific American Mind and Spektrum der Wissenschaft in Germany.

Throughout all its businesses NPG is dedicated to serving the scientific and medical communities and the wider scientifically interested general public. Part of Macmillan Publishers Limited, NPG is a global company with principal offices in London, New York and Tokyo, and offices in cities worldwide including Boston, Buenos Aires, Delhi, Hong Kong, Madrid, Barcelona, Munich, Heidelberg, Basingstoke, Melbourne, Paris, San Francisco, Seoul and Washington DC. For more information, please go to

Published: 04 Mar 2012

Contact details:

The Macmillan Building, 4 Crinan Street
N1 9XW
United Kingdom

+44 20 7833 4000
News topics: 
Content type: 
Websites: Nature press site